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J Biol Chem, Vol. 274, Issue 31, 21932-21936, July 30, 1999
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From BID is a member of the BH3-only subgroup of Bcl-2
family proteins that displays pro-apoptotic activity. The
NH2-terminal region of BID contains a caspase-8
(Casp-8) cleavage site and the cleaved form of BID translocates to
mitochondrial membranes where it is a potent inducer of cytochrome
c release. Secondary structure and fold predictions suggest
that BID has a high degree of The Burnham Institute, La Jolla, California
92307 and the Neuropsychiatric Institute and West Los Angeles
Department of Veterans Affairs Medical Center School of Medicine,
University of California, Los Angeles, California 90024
-helical content and structural
similarity to Bcl-XL, which itself is highly similar to
bacterial pore-forming toxins. Moreover, circular dichroism analysis
confirmed a high -helical content of BID. Amino-terminal truncated
BID
1-55, mimicking the Casp-8-cleaved molecule, formed channels in
planar bilayers at neutral pH and in liposomes at acidic pH. In
contrast, full-length BID displayed channel activity only at
nonphysiological pH 4.0 (but not at neutral pH) in planar bilayers and
failed to form channels in liposomes even under acidic conditions. On a
single channel level, BID1-55 channels were voltage-gated and
exhibited multiconductance behavior at neutral pH. When full-length BID
was cleaved by Casp-8, it too demonstrated channel activity similar to
that seen with BID1-55. Thus, BID appears to share structural and
functional similarity with other Bcl-2 family proteins known to have
channel-forming activity, but its activity exhibits a novel form of
activation: proteolytic cleavage.
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